trichostatin A

Trichostatin is a lipid of Polyketides (PK) class. Trichostatin is associated with abnormalities such as Dentatorubral-Pallidoluysian Atrophy, PARAGANGLIOMAS 3, abnormal fragmented structure, Disintegration (morphologic abnormality) and Hyperostosis, Diffuse Idiopathic Skeletal. The involved functions are known as Acetylation, Cell Differentiation process, histone modification, Gene Silencing and Transcriptional Activation. Trichostatin often locates in CD41a, Hematopoietic System, Chromatin Structure, Blood and Endothelium. The associated genes with Trichostatin are SPI1 gene, CELL Gene, Chromatin, CXCR4 gene and DNMT1 gene. The related lipids are Butyrates, Promega, butyrate, Lipopolysaccharides and Steroids. The related experimental models are Knock-out, Mouse Model, Xenograft Model and Cancer Model.

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Introduction

To understand associated biological information of trichostatin A, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.

What diseases are associated with trichostatin A?

trichostatin A is suspected in Infection, Morphologically altered structure, Ureteral obstruction, Photosensitization, Atherosclerosis, Hypertrophic Cardiomyopathy and other diseases in descending order of the highest number of associated sentences.

Related references are mostly published in these journals:

Disease Cross reference Weighted score Related literature
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Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with trichostatin A

MeSH term MeSH ID Detail
Bone Marrow Neoplasms D019046 2 associated lipids
Carcinoma, Pancreatic Ductal D021441 6 associated lipids
Cat Diseases D002371 12 associated lipids
Biliary Tract Neoplasms D001661 7 associated lipids
Neurodegenerative Diseases D019636 32 associated lipids
Polycystic Kidney, Autosomal Dominant D016891 6 associated lipids
Ventricular Remodeling D020257 28 associated lipids
Endometrial Neoplasms D016889 30 associated lipids
Retinoblastoma D012175 12 associated lipids
Genomic Instability D042822 7 associated lipids
Cicatrix, Hypertrophic D017439 4 associated lipids
Carcinoma, Embryonal D018236 8 associated lipids
Mastocytoma D034801 3 associated lipids
Cell Transformation, Viral D002472 26 associated lipids
Nasopharyngeal Neoplasms D009303 4 associated lipids
Fragile X Syndrome D005600 5 associated lipids
Adenocarcinoma, Follicular D018263 3 associated lipids
Hypereosinophilic Syndrome D017681 3 associated lipids
Retinal Neoplasms D019572 3 associated lipids
Progeria D011371 3 associated lipids
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PubChem Associated disorders and diseases

What pathways are associated with trichostatin A

Lipid pathways are not clear in current pathway databases. We organized associated pathways with trichostatin A through full-text articles, including metabolic pathways or pathways of biological mechanisms.

Related references are published most in these journals:

Pathway name Related literatures
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PubChem Biomolecular Interactions and Pathways

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with trichostatin A?

Related references are published most in these journals:

Location Cross reference Weighted score Related literatures
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What functions are associated with trichostatin A?


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Function Cross reference Weighted score Related literatures

What lipids are associated with trichostatin A?

Related references are published most in these journals:

Lipid concept Cross reference Weighted score Related literatures
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What genes are associated with trichostatin A?

Related references are published most in these journals:


Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with trichostatin A?

Mouse Model

Mouse Model are used in the study 'Regulation of minichromosome maintenance gene family by microRNA-1296 and genistein in prostate cancer.' (Majid S et al., 2010), Mouse Model are used in the study 'Reversal of hypermethylation and reactivation of p16INK4a, RARbeta, and MGMT genes by genistein and other isoflavones from soy.' (Fang MZ et al., 2005) and Mouse Model are used in the study 'Histone deacetylase 3 mediates allergic skin inflammation by regulating expression of MCP1 protein.' (Kim Y et al., 2012).

Xenograft Model

Xenograft Model are used in the study 'Histone deacetylase inhibitors induce growth arrest and differentiation in uveal melanoma.' (Landreville S et al., 2012), Xenograft Model are used in the study 'Extended treatment with physiologic concentrations of dietary phytochemicals results in altered gene expression, reduced growth, and apoptosis of cancer cells.' (Moiseeva EP et al., 2007) and Xenograft Model are used in the study 'Retinoic acid and the histone deacetylase inhibitor trichostatin a inhibit the proliferation of human renal cell carcinoma in a xenograft tumor model.' (Touma SE et al., 2005).

Cancer Model

Cancer Model are used in the study 'Plasma pharmacokinetics and metabolism of the histone deacetylase inhibitor trichostatin a after intraperitoneal administration to mice.' (Sanderson L et al., 2004).

Related references are published most in these journals:

Model Cross reference Weighted score Related literatures
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NCBI Entrez Crosslinks

All references with trichostatin A

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Per page 10 20 50 100 | Total 3126
Authors Title Published Journal PubMed Link
Schmidt K et al. Inhibitors of histone deacetylase suppress the growth of MCF-7 breast cancer cells. 1999 Arch. Pharm. (Weinheim) pmid:10575368
Jung M et al. Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation. 1999 J. Med. Chem. pmid:10579829
Chien PY et al. A fusion protein of the estrogen receptor (ER) and nuclear receptor corepressor (NCoR) strongly inhibits estrogen-dependent responses in breast cancer cells. 1999 Mol. Endocrinol. pmid:10598586
Taddei A et al. Duplication and maintenance of heterochromatin domains. 1999 J. Cell Biol. pmid:10601331
Nielsen AL et al. Interaction with members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in transcriptional silencing by members of the TIF1 family. 1999 EMBO J. pmid:10562550
Saunders N et al. Histone deacetylase inhibitors as potential anti-skin cancer agents. 1999 Cancer Res. pmid:9927053
O'Neill LP et al. A developmental switch in H4 acetylation upstream of Xist plays a role in X chromosome inactivation. 1999 EMBO J. pmid:10329635
Strouboulis J et al. Transcriptional repression by XPc1, a new Polycomb homolog in Xenopus laevis embryos, is independent of histone deacetylase. 1999 Mol. Cell. Biol. pmid:10330136
Bakin AV and Curran T Role of DNA 5-methylcytosine transferase in cell transformation by fos. 1999 Science pmid:9888853
Verdel A and Khochbin S Identification of a new family of higher eukaryotic histone deacetylases. Coordinate expression of differentiation-dependent chromatin modifiers. 1999 J. Biol. Chem. pmid:9891014
Coffee B et al. Acetylated histones are associated with FMR1 in normal but not fragile X-syndrome cells. 1999 Nat. Genet. pmid:10319871
Xiao H et al. Both Sp1 and Sp3 are responsible for p21waf1 promoter activity induced by histone deacetylase inhibitor in NIH3T3 cells. 1999 J. Cell. Biochem. pmid:10321829
Kosugi H et al. Histone deacetylase inhibitors are the potent inducer/enhancer of differentiation in acute myeloid leukemia: a new approach to anti-leukemia therapy. 1999 Leukemia pmid:10482980
Carmen AA et al. Yeast HOS3 forms a novel trichostatin A-insensitive homodimer with intrinsic histone deacetylase activity. 1999 Proc. Natl. Acad. Sci. U.S.A. pmid:10535926
Rüller S et al. Sensitization of tumor cells to ribotoxic stress-induced apoptotic cell death: a new therapeutic strategy. 1999 Clin. Cancer Res. pmid:10537334
Vanden Berghe W et al. The nuclear factor-kappaB engages CBP/p300 and histone acetyltransferase activity for transcriptional activation of the interleukin-6 gene promoter. 1999 J. Biol. Chem. pmid:10542243
Ng HH et al. MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex. 1999 Nat. Genet. pmid:10471499
Sowa Y et al. Sp3, but not Sp1, mediates the transcriptional activation of the p21/WAF1/Cip1 gene promoter by histone deacetylase inhibitor. 1999 Cancer Res. pmid:10485470
Finnin MS et al. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. 1999 Nature pmid:10490031
Huang Y et al. Transcriptional repression by REST: recruitment of Sin3A and histone deacetylase to neuronal genes. 1999 Nat. Neurosci. pmid:10491605